Global InformationCaspase 3 information
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| Aliases | CASP3, CPP32, CPP32B, SCA-1, caspase 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 600636 MGI: 107739 HomoloGene: 37912 GeneCards: CASP3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Caspase-3 is a caspase protein that interacts with caspase-8 and caspase-9. It is encoded by the CASP3 gene. CASP3 orthologs[4] have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.
The CASP3 protein is a member of the cysteine-aspartic acid protease (caspase) family.[5] Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6 and 7; and the protein itself is processed and activated by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease.[6] Alternative splicing of this gene results in two transcript variants that encode the same protein.[7]
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Caspase-3 shares many of the typical characteristics common to all currently-known caspases. For example, its active site contains a cysteine residue (Cys-163) and histidine residue (His-121) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid sequence.[9][10] This specificity allows caspases to be incredibly selective, with a 20,000-fold preference for aspartic acid over glutamic acid.[11] A key feature of caspases in the cell is that they are present as zymogens, termed procaspases, which are inactive until a biochemical change causes their activation. Each procaspase has an N-terminal large subunit of about 20 kDa followed by a smaller subunit of about 10 kDa, called p20 and p10, respectively.[12]
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031628 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "OrthoMaM phylogenetic marker: CASP3 coding sequence". Archived from the original on 2016-03-03. Retrieved 2009-12-20.
- ^ Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA, Wong WW, Yuan J (October 1996). "Human ICE/CED-3 protease nomenclature". Cell. 87 (2): 171. doi:10.1016/S0092-8674(00)81334-3. PMID 8861900. S2CID 5345060.
- ^ Gervais FG, Xu D, Robertson GS, Vaillancourt JP, Zhu Y, Huang J, LeBlanc A, Smith D, Rigby M, Shearman MS, Clarke EE, Zheng H, Van Der Ploeg LH, Ruffolo SC, Thornberry NA, Xanthoudakis S, Zamboni RJ, Roy S, Nicholson DW (April 1999). "Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation". Cell. 97 (3): 395–406. doi:10.1016/s0092-8674(00)80748-5. PMID 10319819. S2CID 17524567.
- ^ "Entrez Gene: CASP3 caspase 3, apoptosis-related cysteine peptidase".
- ^ Harrington HA, Ho KL, Ghosh S, Tung KC (2008). "Construction and analysis of a modular model of caspase activation in apoptosis". Theoretical Biology & Medical Modelling. 5 (1): 26. doi:10.1186/1742-4682-5-26. PMC 2672941. PMID 19077196.
- ^ Wyllie AH (1997). "Apoptosis: an overview". British Medical Bulletin. 53 (3): 451–65. doi:10.1093/oxfordjournals.bmb.a011623. PMID 9374030.
- ^ Perry DK, Smyth MJ, Stennicke HR, Salvesen GS, Duriez P, Poirier GG, Hannun YA (July 1997). "Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis". The Journal of Biological Chemistry. 272 (30): 18530–3. doi:10.1074/jbc.272.30.18530. PMID 9228015.
- ^ Stennicke HR, Renatus M, Meldal M, Salvesen GS (September 2000). "Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8". The Biochemical Journal. 350 (2): 563–8. doi:10.1042/0264-6021:3500563. PMC 1221285. PMID 10947972.
- ^ Salvesen GS (January 2002). "Caspases: opening the boxes and interpreting the arrows". Cell Death and Differentiation. 9 (1): 3–5. doi:10.1038/sj.cdd.4400963. PMID 11803369. S2CID 31274387.